5OHS

A GH31 family sulfoquinovosidase mutant D455N in complex with pNPSQ

Summary for 5OHS

• Entry DOI: 10.2210/pdb5ohs/pdb
• Descriptor: Alpha-glucosidase yihQ, THIOCYANATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (8 entities in total)
• Functional Keywords: sulfoglycosidase, sulfoglycolysis, complex, general acid-base varient, hydrolase
• Biological source: Rhizobium radiobacter (Agrobacterium tumefaciens)
• Total number of polymer chains: 8
• Total formula weight: 607710.37

Authors

Jin, Y.,Williams, S.J.,Goddard-Borger, E.,Davies, G.J. (deposition date: 2017-07-18, release date: 2018-08-08, Last modification date: 2024-05-01)

Primary citation

Abayakoon, P.,Jin, Y.,Lingford, J.P.,Petricevic, M.,John, A.,Ryan, E.,Wai-Ying Mui, J.,Pires, D.E.V.,Ascher, D.B.,Davies, G.J.,Goddard-Borger, E.D.,Williams, S.J.
Structural and Biochemical Insights into the Function and Evolution of Sulfoquinovosidases.
ACS Cent Sci, 4:1266-1273, 2018

PubMed Abstract: An estimated 10 billion tonnes of sulfoquinovose (SQ) are produced and degraded each year. Prokaryotic sulfoglycolytic pathways catabolize sulfoquinovose (SQ) liberated from plant sulfolipid, or its delipidated form α-d-sulfoquinovosyl glycerol (SQGro), through the action of a sulfoquinovosidase (SQase), but little is known about the capacity of SQ glycosides to support growth. Structural studies of the first reported SQase ( YihQ) have identified three conserved residues that are essential for substrate recognition, but crossover mutations exploring active-site residues of predicted SQases from other organisms have yielded inactive mutants casting doubt on bioinformatic functional assignment. Here, we show that SQGro can support the growth of on par with d-glucose, and that the SQase prefers the naturally occurring diastereomer of SQGro. A predicted, but divergent, SQase from proved to have highly specific activity toward SQ glycosides, and structural, mutagenic, and bioinformatic analyses revealed the molecular coevolution of catalytically important amino acid pairs directly involved in substrate recognition, as well as structurally important pairs distal to the active site. Understanding the defining features of SQases empowers bioinformatic approaches for mapping sulfur metabolism in diverse microbial communities and sheds light on this poorly understood arm of the biosulfur cycle.

PubMed: 30276262
DOI: 10.1021/acscentsci.8b00453

Experimental method

X-RAY DIFFRACTION (1.97 Å)